Extracellular Proteases in Erwinia chrysanthemi
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چکیده
منابع مشابه
Lactose metabolism in Erwinia chrysanthemi.
Wild-type strains of the phytopathogenic enterobacterium Erwinia chrysanthemi are unable to use lactose as a carbon source for growth although they possess a beta-galactosidase activity. Lactose-fermenting derivatives from some wild types, however, can be obtained spontaneously at a frequency of about 5 X 10(-7). All Lac+ derivatives isolated had acquired a constitutive lactose transport system...
متن کاملLactose and melibiose metabolism in Erwinia chrysanthemi.
A Lac+ mutant of Erwinia chrysanthemi was isolated from the Lac- wild type on lactose agar. beta-Galactosidase was expressed independently of lactose transport in both the mutant and the wild type, and neither strain expressed thiogalactoside transacetylase. Lactose transport and alpha-galactosidase, constitutive in the Lac+ strain, were coordinately induced in the Lac- strain by melibiose and ...
متن کاملGeneralized transduction in the enterobacterial phytopathogen Erwinia chrysanthemi.
Bacteriophages induced by mitomycin treatment of Erwinia chrysanthemi KS612 produced plaques on lawns of E. chrysanthemi EC183 and KS605. Bacteriophage Erch-12, purified from one such plaque, transferred an array of chromosomal genes (arg, leu, his, ser, thr, trp, ura) to appropriate recipient strains derived from E. chrysanthemi EC 183. Recombinants were formed in the absence of cellular conta...
متن کاملUptake of galacturonic acid in Erwinia chrysanthemi EC16.
Uptake of [14C]galacturonic acid in Erwinia chrysanthemi was found to be stimulated during growth on pectin and its degradation products, saturated digalacturonic acid and galacturonic acid. Cells isolated from macerated potato tissue also showed increased levels of uptake activity for this molecule compared with those showed by glycerol-grown cells. Uptake was found to be an active process, an...
متن کاملProtease secretion by Erwinia chrysanthemi. Proteases B and C are synthesized and secreted as zymogens without a signal peptide.
The gene encoding the secreted 53-kDa metalloprotease (protease B) and the 5' end of the gene encoding the secreted 55-kDa metalloprotease (protease C) of the Gram-negative bacterium Erwinia chrysanthemi have been sequenced. The predicted sequences of the two proteases do not have typical signal sequences at their NH2 termini. Both proteases are synthesized as inactive higher molecular weight p...
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ژورنال
عنوان ژورنال: Microbiology
سال: 1986
ISSN: 1350-0872,1465-2080
DOI: 10.1099/00221287-132-4-899